Isolation from haemolysate of a proteinaceous inhibition of the red cell Ca2+-pump ATPase. Its action on the kinetics of the enzyme.

The purification to apparent homogeneity of a small protein from the cytosol of human red cells is described. The procedure consists of a combination of anion-exchange-chromatography, ultrafiltration, (NH4)2SO4- and heat-precipitation. The resulting protein is a potent inhibitor of (Ca2+ + Mg2+)-ATPase of erythrocyte membranes and of Ca2+-uptake into inside-out vesicles. Membrane (Na+ + K+)-ATPase is not affected by the inhibitor. The peptide migrates as a single band in SDS gels. Its apparent molecular weight is 19,000. It causes inhibition of the Ca2+-pump by decreasing Ca2+-affinity at all calmodulin concentrations.